ArticleProceedings of the National Academy of Sciences of the United States of America2016
X-ray and cryo-EM structures of monomeric and filamentous actin-like protein MamK reveal changes associated with polymerization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Article
- Biosynthesis and function of magnetic organelles in magnetotactic bacteria.Nature reviews. Microbiology · 2026Review
- Visualizing the dynamic polymerization of the bacterial actin-like cytoskeleton for magnetic organelle positioning.Scientific reports · 2025Article
- Magnetosome organelles are organized through interactions between McaA and McaB that alter the dynamics of the bacterial actin-like protein MamK.bioRxiv : the preprint server for biology · 2025Article
- A family of bacterial actin homologs forms a three-stranded tubular structure.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Filament organization of the bacterial actin MreB is dependent on the nucleotide state.The Journal of cell biology · 2022Article
- A Compass To Boost Navigation: Cell Biology of Bacterial Magnetotaxis.Journal of bacteriology · 2020Review
- Polymerization in the actin ATPase clan regulates hexokinase activity in yeast.Science (New York, N.Y.) · 2020Article
- Cryo-EM Structure of Actin Filaments fromThe Plant cell · 2019Article
- Cryo-EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution.FEBS letters · 2019Article
- Prokaryotic cytoskeletons: protein filaments organizing small cells.Nature reviews. Microbiology · 2018Review
- Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cryo-EM reconstruction of AlfA fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Evolution of polymer formation within the actin superfamily.Molecular biology of the cell · 2017Review
- Helical reconstruction in RELION.Journal of structural biology · 2017Article
- Article
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Abstract
Magnetotactic bacteria produce iron-rich magnetic nanoparticles that are enclosed by membrane invaginations to form magnetosomes so they are able to sense and act upon Earth's magnetic field. In Magnetospirillum and other magnetotactic bacteria, to combine their magnetic moments, magnetosomes align along filaments formed by a bacterial actin homolog, MamK. Here, we present the crystal structure of a nonpolymerizing mutant of MamK from Magnetospirillum magneticum AMB-1 at 1.8-Å resolution, revealing its close similarity to actin and MreB. The crystals contain AMPPNP-bound monomeric MamK in two different conformations. To investigate conformational changes associated with polymerization, we used unmodified MamK protein and cryo-EM with helical 3D reconstruction in RELION to obtain a density map and a fully refined atomic model of MamK in filamentous form at 3.6-Å resolution. The filament is parallel (polar) double-helical, with a rise of 52.2 Å and a twist of 23.8°. As shown previously and unusually for actin-like filaments, the MamK subunits from each of the two strands are juxtaposed, creating an additional twofold axis along the filament. Compared with monomeric MamK, ADP-bound MamK in the filament undergoes a conformational change, rotating domains I and II against each other to further close the interdomain cleft between subdomains IB and IIB. The domain movement causes several loops to close around the nucleotide-binding pocket. Glu-143, a key residue for catalysis coordinating the magnesium ion, moves closer, presumably switching nucleotide hydrolysis upon polymerization-one of the hallmarks of cytomotive filaments of the actin type.
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